Niobium nitride films formed by rapid thermal processing (RTP): a study of depth profiles and interface reactions by complementary analytical techniques.

The nitridation of niobium films approximately 250 and 650 nm thick by rapid thermal processing (RTP) at 800 degrees C in molecular nitrogen or ammonia was investigated. The niobium films were deposited by electron beam evaporation on silicon substrates covered by a 100 or 300 nm thick thermally grown SiO(2) layer. In these investigations the reactivity of ammonia and molecular nitrogen was compared with regard to nitride formation and reaction with the SiO(2) substrate layer. The phases formed were characterized by X-ray diffraction (XRD). Depth profiles of the elements in the films were recorded by use of secondary neutral mass spectrometry (SNMS). Microstructure and spatial distribution of the elements were imaged by transmission electron microscopy (TEM) and energy-filtered TEM (EFTEM). Electron energy loss spectra (EELS) were taken at selected positions to discriminate between different nitride, oxynitride, and oxide phases. The results provide clear evidence of the expected higher reactivity of ammonia in nitride formation and reaction with the SiO(2) substrate layer. Outdiffusion of oxygen into the niobium film and indiffusion of nitrogen from the surface of the film result in the formation of oxynitride in a zone adjacent to the Nb/SiO(2) interface. SNMS profiles of nitrogen reveal a distinct tail which is attributed to enhanced diffusion of nitrogen along grain boundaries.

The fla gene cluster is involved in the biogenesis of flagella in Halobacterium salinarum.

In this study, a flagella-related protein gene cluster is described for Halobacterium salinarum. The fla gene cluster is located upstream of the flagellin genes flgB1-3 and oriented in the opposite direction. It consists of nine open reading frames (ORFs): htpIX, a member of the halobacterial transducer protein gene family, and the genes flaD-K. The genes flaD, E, G, H, I and J share high homologies with genes from other Archaea. Interestingly, flaK shows similarities to bacterial genes involved in the regulation of flagellar synthesis. The ORFs of flaH, flaI and flaK contain sequences coding for nucleotide binding sites. Furthermore, flaI contains a motif called the bacterial type II secretion protein E signature, indicating a functional relation to members of the bacterial pili type IV-type II secretion protein superfamily. Reverse transcription-polymerase chain reaction (RT-PCR) analysis revealed that the genes flaE to flaK are transcribed into one polycistronic message. In frame deletion mutants of flaI were generated by gene replacement. The deletion strain lacks motility and belongs to the fla(-) mutant class, indicating that it is deficient in flagellar biogenesis. The overall amount of flagellin protein in Delta flaI cells is reduced, although transcription of the flagellin genes is unaffected. Therefore, the flaI gene product is involved in the biosynthesis, transport or assembly of flagella in H. salinarum.